| An evolutionarily conserved fission yeast protein, Ned1, implicated in normal nuclear morphology and chromosome stability, interacts with Dis3, Pim1/RCC1 and an essential nucleoporin. | |
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MedLine Citation:
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PMID: 12376568 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We identified a novel fission yeast gene, ned1(+), with pleiotropic mutations that have a high incidence of chromosome missegregation, aberrantly shaped nuclei, overdeveloped endoplasmic reticulum-like membranes, and increased sensitivity to a microtubule destabilizing agent. Ned1 protein, which was phosphorylated in a growth-related manner, interacted in a yeast two-hybrid system with Dis3 as well as with Pim1/RCC1 (nucleotide exchange factor for Ran). Ned1 also interacted with an essential nucleoporin, a probable homologue of mammalian Nup98/96. The ned1 gene displayed a variety of genetic interactions with factors involved in nuclear transport and chromosome segregation, including the crm1 (exportin), spi1 (small GTPase Ran), pim1, and dis genes. A substitution mutation that affected the two-hybrid interaction with Dis3 increased chromosome instability, suggesting the functional importance of the interaction. Overproduction of Ned1 protein induced formation of an abnormal microtubule bundle within the nucleus, apparently independently of the spindle pole body, but dependent on pim1(+) activity. The ned1(+) gene belongs to an evolutionarily conserved gene family, which includes the mouse Lpin genes, one of whose mutations is responsible for lipodystrophy. |
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Authors:
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Yoshie Tange; Aiko Hirata; Osami Niwa |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of cell science Volume: 115 ISSN: 0021-9533 ISO Abbreviation: J. Cell. Sci. Publication Date: 2002 Nov |
Date Detail:
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Created Date: 2002-10-11 Completed Date: 2003-07-02 Revised Date: 2009-12-11 |
Medline Journal Info:
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Nlm Unique ID: 0052457 Medline TA: J Cell Sci Country: England |
Other Details:
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Languages: eng Pagination: 4375-85 Citation Subset: IM |
Affiliation:
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Kazusa DNA Research Institute, 2-6-7 Kazusa-kamatari, Kisarazu, Chiba 292-0818, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Active Transport, Cell Nucleus
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genetics Amino Acid Sequence / genetics Base Sequence / genetics Chromosome Segregation / genetics Cloning, Molecular DNA, Complementary / analysis, genetics Evolution, Molecular Exoribonucleases Fungal Proteins / genetics, metabolism Gene Expression Regulation, Fungal / genetics Guanine Nucleotide Exchange Factors* Microscopy, Electron Microtubules / genetics, metabolism, pathology Molecular Sequence Data Mutation / genetics Nuclear Envelope / genetics, metabolism*, pathology Nuclear Pore Complex Proteins / genetics, metabolism Nuclear Proteins / genetics, isolation & purification*, metabolism Phosphatidate Phosphatase Phylogeny Saccharomyces cerevisiae / genetics, metabolism*, ultrastructure Saccharomyces cerevisiae Proteins / genetics, isolation & purification*, metabolism Schizosaccharomyces / genetics, metabolism*, ultrastructure Schizosaccharomyces pombe Proteins / genetics, isolation & purification* Serine Endopeptidases / genetics, metabolism |
| Chemical | |
Reg. No./Substance:
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0/DNA, Complementary; 0/Fungal Proteins; 0/Guanine Nucleotide Exchange Factors; 0/Ned1 protein, S pombe; 0/Nuclear Pore Complex Proteins; 0/Nuclear Proteins; 0/Saccharomyces cerevisiae Proteins; 0/Schizosaccharomyces pombe Proteins; 0/pim1 protein, S pombe; EC 3.1.-/Exoribonucleases; EC 3.1.13.-/DIS3 protein, S cerevisiae; EC 3.1.13.-/dis3 protein, S pombe; EC 3.1.3.4/Phosphatidate Phosphatase; EC 3.1.3.4/SMP2 protein, S cerevisiae; EC 3.4.21.-/Serine Endopeptidases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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